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7UV9

KDM2A-nucleosome structure stabilized by H3K36C-UNC8015 covalent conjugate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000785cellular_componentchromatin
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0010467biological_processgene expression
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
A0070062cellular_componentextracellular exosome
B0000781cellular_componentchromosome, telomeric region
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0016020cellular_componentmembrane
B0030527molecular_functionstructural constituent of chromatin
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0043505cellular_componentCENP-A containing nucleosome
B0045653biological_processnegative regulation of megakaryocyte differentiation
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
B0070062cellular_componentextracellular exosome
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0019899molecular_functionenzyme binding
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
C0046982molecular_functionprotein heterodimerization activity
C0070062cellular_componentextracellular exosome
D0000786cellular_componentnucleosome
D0002227biological_processinnate immune response in mucosa
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0005829cellular_componentcytosol
D0006334biological_processnucleosome assembly
D0019731biological_processantibacterial humoral response
D0030527molecular_functionstructural constituent of chromatin
D0042742biological_processdefense response to bacterium
D0042802molecular_functionidentical protein binding
D0046982molecular_functionprotein heterodimerization activity
D0050830biological_processdefense response to Gram-positive bacterium
D0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
D0070062cellular_componentextracellular exosome
E0000122biological_processnegative regulation of transcription by RNA polymerase II
E0000785cellular_componentchromatin
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0003682molecular_functionchromatin binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0010467biological_processgene expression
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
E0070062cellular_componentextracellular exosome
F0000781cellular_componentchromosome, telomeric region
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0003723molecular_functionRNA binding
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0016020cellular_componentmembrane
F0030527molecular_functionstructural constituent of chromatin
F0032200biological_processtelomere organization
F0032991cellular_componentprotein-containing complex
F0043505cellular_componentCENP-A containing nucleosome
F0045653biological_processnegative regulation of megakaryocyte differentiation
F0046982molecular_functionprotein heterodimerization activity
F0061644biological_processprotein localization to CENP-A containing chromatin
F0070062cellular_componentextracellular exosome
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0019899molecular_functionenzyme binding
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
G0070062cellular_componentextracellular exosome
H0000786cellular_componentnucleosome
H0002227biological_processinnate immune response in mucosa
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005615cellular_componentextracellular space
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0005829cellular_componentcytosol
H0006334biological_processnucleosome assembly
H0019731biological_processantibacterial humoral response
H0030527molecular_functionstructural constituent of chromatin
H0042742biological_processdefense response to bacterium
H0042802molecular_functionidentical protein binding
H0046982molecular_functionprotein heterodimerization activity
H0050830biological_processdefense response to Gram-positive bacterium
H0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
H0070062cellular_componentextracellular exosome
K0003677molecular_functionDNA binding
K0008270molecular_functionzinc ion binding
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CVQGECGVC
ChainResidueDetails
KCYS577-CYS585

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG92-GLY114

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

site_idPS01359
Number of Residues56
DetailsZF_PHD_1 Zinc finger PHD-type signature. CslCgevdqneetqdfekklm............................EcCi...Cnei.VHpgClqmdgegllneelpnc.............................WeCpkC
ChainResidueDetails
KCYS620-CYS675

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsZN_FING: CXXC-type => ECO:0000255|PROSITE-ProRule:PRU00509, ECO:0007744|PDB:4BBQ
ChainResidueDetails
KALA564-LEU610
HPRO1

site_idSWS_FT_FI2
Number of Residues61
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146, ECO:0007744|PDB:4BBQ
ChainResidueDetails
KSER617-GLU678
HGLU2

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
KTHR209
HLYS11
HLYS15
HLYS16
HLYS20
HLYS23
HLYS43
HLYS85
KLYS229
DLYS15
DLYS16
DLYS20
DLYS23
DLYS43
DLYS85
HLYS5

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:16362057, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2
ChainResidueDetails
KHIS212
HSER6
GLYS9
GLYS95

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|Ref.27, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2
ChainResidueDetails
KASP214
KHIS284
BLYS44
FLYS8
FLYS16
FLYS44

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00509, ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ
ChainResidueDetails
KCYS571
KCYS574
KCYS577
KCYS582
KCYS585
KCYS588
KCYS604
KCYS609

site_idSWS_FT_FI7
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ
ChainResidueDetails
KCYS620
KCYS623
KCYS642
KCYS645
KHIS650
KCYS653
KCYS672
KCYS675

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
KSER28
DLYS116
DLYS120
HLYS34
HLYS116
HLYS120

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
KSER390
HGLU35
CLYS125
GLYS118
GLYS119
GLYS125

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
KSER394
HSER36
ELYS14
ELYS56

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
KTHR550
DLYS108
HLYS46
HLYS108

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
KSER558
HLYS57
GLYS119

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17525332
ChainResidueDetails
KTHR632
HARG79

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
KLYS505
DARG92
HARG86
HARG92

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DTHR115
HTHR115
FLYS91

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020
ChainResidueDetails
DSER112
HSER112
BLYS79
FLYS20
FLYS59
FLYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876
ChainResidueDetails
DLYS5
HLYS5

site_idSWS_FT_FI18
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:22121020
ChainResidueDetails
ASER57
DLYS120
HLYS120

site_idSWS_FT_FI19
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6
ChainResidueDetails
DLYS20
HLYS20

site_idSWS_FT_FI20
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
DLYS34
HLYS34

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR107
ETHR107

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI25
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ALYS18
ELYS18

site_idSWS_FT_FI26
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21076176
ChainResidueDetails
AALA110
EALA110

237423

PDB entries from 2025-06-11

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